Ubiquitination of aquaporin-2 in the kidney

Yu Jung Lee, Tae Hwan Kwon

Research output: Contribution to journalReview articlepeer-review

9 Scopus citations

Abstract

Ubiquitination is known to be important for endocytosis and lysosomal degradation of aquaporin-2 (AQP2). Ubiquitin (Ub) is covalently attached to the lysine residue of the substrate proteins and activation and attachment of Ub to a target protein is mediated by the action of three enzymes (i.e., E1, E2, and E3). In particular, E3 Ub-protein ligases are known to have substrate specificity. This minireview will discuss the ubiquitination of AQP2 and identification of potential E3 Ub-protein ligases for 1-deamino-8-D-arginine vasopressin (dDAVP)-dependent AQP2 regulation.

Original languageEnglish
Pages (from-to)1-4
Number of pages4
JournalElectrolyte and Blood Pressure
Volume7
Issue number1
DOIs
StatePublished - Jun 2009

Keywords

  • Aquaporin 2
  • Collecting
  • Kidney tubules
  • Ubiquitination
  • Vasopressins

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